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Items: 1 to 20 of 528

1.
The Evolution of Genetic Variability at the LRRK2 Locus
Dylan T. Guenther, Jordan Follett, Rim Amouri, Samia Ben Sassi, Faycel Hentati, Matthew J. Farrer
Genes (Basel) 2024 Jul; 15(7): 878. Published online 2024 Jul 3. doi: 10.3390/genes15070878
PMCID:
PMC11275506
AbstractArticlePDF–1.0M
2.
Genetic analysis and natural history of Parkinson’s disease due to the LRRK2 G2019S variant
Matthew J Kmiecik, Steven Micheletti, Daniella Coker, Karl Heilbron, Jingchunzi Shi, Keaton Stagaman, Teresa Filshtein Sonmez, Pierre Fontanillas, Suyash Shringarpure, Madeleine Wetzel, Helen M Rowbotham, Paul Cannon, Janie F Shelton, David A Hinds, Joyce Y Tung, 23andMe Research Team , Michael V Holmes, Stella Aslibekyan, Lucy Norcliffe-Kaufmann
Brain. 2024 Jun; 147(6): 1996–2008. Published online 2024 May 28. doi: 10.1093/brain/awae073
PMCID:
PMC11146432
AbstractArticlePDF–855K
3.
The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK/ERK pathway
José M. Bravo-San Pedro, Mireia Niso-Santano, Rubén Gómez-Sánchez, Elisa Pizarro-Estrella, Ana Aiastui-Pujana, Ana Gorostidi, Vicente Climent, Rakel López de Maturana, Rosario Sanchez-Pernaute, Adolfo López de Munain, José M. Fuentes, Rosa A. González-Polo
Cell Mol Life Sci. 2013 Jan; 70(1): 121–136. Published online 2012 Jul 8. doi: 10.1007/s00018-012-1061-y
PMCID:
PMC11113213
AbstractArticlePDF–1.0M
4.
Sex-dependent interactions between prodromal intestinal inflammation and LRRK2 G2019S in mice promote endophenotypes of Parkinson’s disease
Ping Fang, Lewis W. Yu, Hannah Espey, Gulistan Agirman, Sabeen A. Kazmi, Kai Li, Yongning Deng, Jamie Lee, Haley Hrncir, Arlene Romero-Lopez, Arthur P. Arnold, Elaine Y. Hsiao
Commun Biol. 2024; 7: 570. Published online 2024 May 15. doi: 10.1038/s42003-024-06256-9
PMCID:
PMC11096388
AbstractArticlePDF–4.6M
5.
Multi-tracer PET correlation analysis reveals disease-specific patterns in Parkinson’s disease and asymptomatic LRRK2 pathogenic variant carriers compared to healthy controls
Julia G. Mannheim, Jessie Fanglu Fu, Tilman Wegener, Ivan S. Klyuzhin, Nasim Vafai, Elham Shahinfard, Jessamyn McKenzie, Audrey Strongosky, Zbigniew K. Wszolek, A. Jon Stoessl, Vesna Sossi
Neuroimage Clin. 2024; 42: 103600. Published online 2024 Apr 1. doi: 10.1016/j.nicl.2024.103600
PMCID:
PMC11015486
AbstractArticlePDF–2.7M
6.
RAB3 phosphorylation by pathogenic LRRK2 impairs trafficking of synaptic vesicle precursors
Dan Dou, Jayne Aiken, Erika L.F. Holzbaur
J Cell Biol. 2024 Jun 3; 223(6): e202307092. Published online 2024 Mar 21. doi: 10.1083/jcb.202307092
PMCID:
PMC10959120
AbstractArticlePDF–5.4M
7.
The LRRK2 kinase substrates RAB8a and RAB10 contribute complementary but distinct disease-relevant phenotypes in human neurons
Adamantios Mamais, Anwesha Sanyal, Austin Fajfer, Catherine G. Zykoski, Michael Guldin, Alexis Riley-DiPaolo, Nitya Subrahmanian, Whitney Gibbs, Steven Lin, Matthew J. LaVoie
Stem Cell Reports. 2024 Feb 13; 19(2): 163–173. Published online 2024 Feb 1. doi: 10.1016/j.stemcr.2024.01.001
PMCID:
PMC10874859
AbstractArticlePDF–5.3M
8.
VPS35 and retromer dysfunction in Parkinson's disease
Jordan Rowlands, Darren J. Moore
Philos Trans R Soc Lond B Biol Sci. April 8, 2024; 379(1899): 20220384. Published online February 19, 2024. doi: 10.1098/rstb.2022.0384
PMCID:
PMC10874700
AbstractArticlePDF–578K
9.
Comprehensive analysis of clinical and biological features in Parkinson's disease associated with the LRRK2 G2019S mutation: Data from the PPMI study
Xiaohui Sun, Kaixin Dou, Li Xue, Yijie Xie, Yong Yang, Anmu Xie
Clin Transl Sci. 2024 Jan; 17(1): e13720. Published online 2024 Jan 23. doi: 10.1111/cts.13720
PMCID:
PMC10804919
AbstractArticlePDF–3.5M
10.
The V-ATPase–ATG16L1 axis recruits LRRK2 to facilitate the lysosomal stress response
Tomoya Eguchi, Maria Sakurai, Yingxue Wang, Chieko Saito, Gen Yoshii, Thomas Wileman, Noboru Mizushima, Tomoki Kuwahara, Takeshi Iwatsubo
J Cell Biol. 2024 Mar 4; 223(3): e202302067. Published online 2024 Jan 16. doi: 10.1083/jcb.202302067
PMCID:
PMC10791558
AbstractArticlePDF–5.8M
11.
Human iPSC-derived microglia carrying the LRRK2-G2019S mutation show a Parkinson’s disease related transcriptional profile and function
Sohvi Ohtonen, Luca Giudice, Henna Jäntti, Mohammad Feroze Fazaludeen, Anastasia Shakirzyanova, Mireia Gómez-Budia, Nelli-Noora Välimäki, Jonna Niskanen, Nea Korvenlaita, Ilkka Fagerlund, Jari Koistinaho, Mahmood Amiry-Moghaddam, Ekaterina Savchenko, Laurent Roybon, Šárka Lehtonen, Paula Korhonen, Tarja Malm
Sci Rep. 2023; 13: 22118. Published online 2023 Dec 13. doi: 10.1038/s41598-023-49294-9
PMCID:
PMC10719377
AbstractArticlePDF–3.9M
12.
Rab12 is a regulator of LRRK2 and its activation by damaged lysosomes
Xiang Wang, Vitaliy V Bondar, Oliver B Davis, Michael T Maloney, Maayan Agam, Marcus Y Chin, Audrey Cheuk-Nga Ho, Rajarshi Ghosh, Dara E Leto, David Joy, Meredith EK Calvert, Joseph W Lewcock, Gilbert Di Paolo, Robert G Thorne, Zachary K Sweeney, Anastasia G Henry
eLife. 2023; 12: e87255. Published online 2023 Oct 24. doi: 10.7554/eLife.87255
PMCID:
PMC10708889
AbstractArticlePDF–1.9M
13.
Localization of PPM1H phosphatase tunes Parkinson’s disease-linked LRRK2 kinase-mediated Rab GTPase phosphorylation and ciliogenesis
Wondwossen M. Yeshaw, Ayan Adhikari, Claire Y. Chiang, Herschel S. Dhekne, Paulina S. Wawro, Suzanne R. Pfeffer
Proc Natl Acad Sci U S A. 2023 Oct 31; 120(44): e2315171120. Published online 2023 Oct 27. doi: 10.1073/pnas.2315171120
PMCID:
PMC10622911
AbstractArticlePDF–6.7M
14.
LRRK2 is involved in the chemotaxis of neutrophils and differentiated HL-60 cells, and the inhibition of LRRK2 kinase activity increases fMLP-induced chemotactic activity
Yuichi Mazaki, Haruka Handa, Yoshizuki Fumoto, Takahiro Horinouchi, Yasuhito Onodera
Cell Commun Signal. 2023; 21: 300. Published online 2023 Oct 30. doi: 10.1186/s12964-023-01305-y
PMCID:
PMC10614378
AbstractArticlePDF–1.3M
15.
Differences in EEG Event-Related Potentials during Dual Task in Parkinson’s Disease Carriers and Non-Carriers of the G2019S-LRRK2 Mutation
Eden Shkury, Shani Danziger-Schragenheim, Zoya Katzir, Yael Ezra, Nir Giladi, Anat Mirelman, Inbal Maidan
Sensors (Basel) 2023 Oct; 23(19): 8266. Published online 2023 Oct 6. doi: 10.3390/s23198266
PMCID:
PMC10575245
AbstractArticlePDF–2.0M
16.
Endogenous Rab38 regulates LRRK2’s membrane recruitment and substrate Rab phosphorylation in melanocytes
Alexandra Unapanta, Farbod Shavarebi, Jacob Porath, Yiyi Shen, Carson Balen, Albert Nguyen, Josh Tseng, Weng Si Leong, Michelle Liu, Pawel Lis, Santiago M. Di Pietro, Annie Hiniker
J Biol Chem. 2023 Oct; 299(10): 105192. Published online 2023 Aug 23. doi: 10.1016/j.jbc.2023.105192
PMCID:
PMC10551901
AbstractArticlePDF–4.1M
17.
The Avidity of Autoreactive Alpha-Synuclein Antibodies in Leucine-Rich Repeat Kinase 2 Mutation Carriers Is Not Altered Compared to Healthy Controls or Patients with Parkinson’s Disease
Alexandra Albus, Yannick Kronimus, Monika Burg-Roderfeld, Hendrik van der Wurp, Dieter Willbold, Tamar Ziehm, Richard Dodel, Jean Alexander Ross
Biomolecules. 2023 Sep; 13(9): 1303. Published online 2023 Aug 25. doi: 10.3390/biom13091303
PMCID:
PMC10526238
AbstractArticlePDF–571K
18.
Patterns of TDP-43 Deposition in Brains with LRRK2 G2019S Mutations
Julian Agin-Liebes, Richard A. Hickman, Jean Paul Vonsattel, Phyllis L. Faust, Xena Flowers, Irina Utkina Sosunova, Joel Ntiri, Richard Mayeux, Matthew Surface, Karen Marder, Stanley Fahn, Serge Przedborski, Roy N. Alcalay
Mov Disord. Author manuscript; available in PMC 2024 Aug 1.
Published in final edited form as: Mov Disord. 2023 Aug; 38(8): 1541–1545. Published online 2023 May 23. doi: 10.1002/mds.29449
PMCID:
PMC10524857
AbstractArticlePDF–355K
19.
Leucine-rich repeat kinase 2 at a glance
Christiane Zhu, Susanne Herbst, Patrick A. Lewis
J Cell Sci. 2023 Sep 1; 136(17): jcs259724. Published online 2023 Sep 12. doi: 10.1242/jcs.259724
PMCID:
PMC10508695
AbstractArticle
20.
LRRK2 aggravates kidney injury through promoting MFN2 degradation and abnormal mitochondrial integrity
Shun Zhang, Subo Qian, Hailong Liu, Ding Xu, Weimin Xia, Huangqi Duan, Chen Wang, Shenggen Yu, Yingying Chen, Ping Ji, Shujun Wang, Xingang Cui, Ying Wang, Haibo Shen
Redox Biol. 2023 Oct; 66: 102860. Published online 2023 Aug 22. doi: 10.1016/j.redox.2023.102860
PMCID:
PMC10470420
AbstractArticlePDF–24M

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